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Validated All-in-One™ qPCR Primer for PARN(NM_002582.4) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
The protein encoded by this gene is a 3'-exoribonuclease, with similarity to the RNase D family of 3'-exonucleases. It prefers poly(A) as the substrate, hence, efficiently degrades poly(A) tails of mRNAs. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs. This protein is also involved in silencing of certain maternal mRNAs during oocyte maturation and early embryonic development, as well as in nonsense-mediated decay (NMD) of mRNAs that contain premature stop codons. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].
Gene References into function
- PARN is a poly(A)-specific member of the RNase D family of 3' exoribonucleases. It is distributed between the nucleus and the cytoplasm and is not stably associated with ribosomes. Xenopus PARN catalyzes deadenylation during oocyte maturation.
- Deadenylation by the mammalian and amphibian poly(A)-specific exoribonuclease, PARN, is stimulated by the presence of an m(7)-guanosine cap on substrate RNAs. PARN exhibits intrinsic cap-binding activity.
- PARN binds to the 5' cap on substrate mRNAs. Cap-binding is stimulated by a poly(A) tail and competed by eIF4E. Cap-PARN interactions integrate regulated mRNA stability and translation.
- The m7GpppG cap has multiple effects on PARN activity. In cis, the 5'cap stimulates deadenylation by increasing PARN processivity. In trans, low concentrations of cap stimulate PARN activity whereas high concentrations inhibit deadenylation.
- Xenopus oocytes contain cytoplasmic (p62) and nuclear (p74) isoforms of PARN. p62 is proteolytically derived from p74. Both isoforms are expressed throughout oogenesis and early development.
- residues of human PARN, Asp(28), Glu(30), Asp(292), and Asp(382), are essential for catalysis but are not required for stabilization of the PARN x RNA substrate complex.
- Results show that tristetraprolin can promote the deadenylation of AU-rich element (ARE)-containing, polyadenylated substrates by poly(A) RNase.
- study of binding and coordination of divalent metal ions in the active site of PARN
- The crystal structure of C-terminal truncated human PARN determined in two states (free and RNA-bound forms) reveals that PARN is folded into two domains, an R3H domain and a nuclease domain
- Association of CBC with PARN might have importance in the regulated recruitment of PARN to the nonsense-mediated decay pathway during the pioneer round of translation.
- CUG-BP binds specifically to both of these RNAs and stimulates poly(A) shortening by PARN. Moreover, CUG-BP interacts with PARN in extracts by coimmunoprecipitation, and this interaction can be recapitulated using recombinant proteins
- The entire RNA-recognition motif (RRM) domain not only contributes to the substrate binding and efficient catalysis of PARN, but also stabilizes the overall structures of the protein.
- REsults describe the crystal structure of the poly(A)-specific ribonuclease (PARN)-RRM domain with a bound 7-methylguanosine triphosphate nucleotide, revealing a novel binding mode for the m(7)G cap.
- PARN is an allosteric enzyme, and potassium ions and the cap analogue are effectors with binding sites located at the RRM domain.